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RFC1

Protein FULL name:

Replication factor C subunit 1, Activator 1 subunit 1, Replication factor C large subunit, Replication factor C 140 kDa subunit, Activator 1 140 kDa subunit, Activator 1 large subunit, DNA-binding protein PO-GA.,


Protein SHORT name:

RF-C 140 kDa subunit RFC140 A1 140 kDa subunit


RFC1 (Homo sapiens) is product of expression of RFC1 gene.


RFC1 is involved in:

DDS in Homo sapiens
     
NER in Homo sapiens




FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.

FUNCTION: Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.

SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA.

INTERACTION: P35250:RFC2; NbExp=1; IntAct=EBI-476616, EBI-476409; Q14683:SMC1A; NbExp=1; IntAct=EBI-476616, EBI-80690;

SUBCELLULAR LOCATION: Nucleus.

TISSUE SPECIFICITY: Wide tissue distribution. Undetectable in placental tissue.

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

SIMILARITY: Belongs to the activator 1 large subunit family.

SIMILARITY: Contains 1 BRCT domain.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


This protein can be a part of a given complexes:
NCBI GenPept GI number(s): 56757608
30353858
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P35251 P35251
PFAM: PF00004
PF00533
PF08519
PF00004
PF00533
PF08519
InterPro: IPR003593
IPR003959
IPR001357
IPR008921
IPR012178
IPR013725
IPR003593
IPR003959
IPR001357
IPR008921
IPR012178
IPR013725
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MDIRKFFGVIPSGKKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRK
EDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLPVSSKPGKISR
QDPVTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKT
KNKPLSPIKLTPTSVLDYFGTGSVQRSNKKMVASKRKELSQNTDESGLND
EAIAKQLQLDEDAELERQLHEDEEFARTLAMLDEEPKTKKARKDTEAGET
FSSVQANLSKAEKHKYPHKVKTAQVSDERKSYSPRKQSKYESSKESQQHS
KSSADKIGEVSSPKASSKLAIMKRKEESSYKEIEPVASKRKENAIKLKGE
TKTPKKTKSSPAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIP
KGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVM
GRDSGQSKSDKAAALGTKIIDEDGLLNLIRTMPGKKSKYEIAVETEMKKE
SKLERTPQKNVQGKRKISPSKKESESKKSRPTSKRDSLAKTIKKETDVFW
KSLDFKEQVAEETSGDSKARNLADDSSENKVENLLWVDKYKPTSLKTIIG
QQGDQSCANKLLRWLRNWQKSSSEDKKHAAKFGKFSGKDDGSSFKAALLS
GPPGVGKTTTASLVCQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIK
GFYSNGAASSVSTKHALIMDEVDGMAGNEDRGGIQELIGLIKHTKIPIIC
MCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAM
NEIILGANQDIRQVLHNLSMWCARSKALTYDQAKADSHRAKKDIKMGPFD
VARKVFAAGEETAHMSLVDKSDLFFHDYSIAPLFVQENYIHVKPVAAGGD
MKKHLMLLSRAADSICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMR
GYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLS
LLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWGGKPSP
FSKLDPKVKAAFTRAYNKEAHLTPYSLQAIKASRHSTSPSLDSEYNEELN
EDDSQSDEKDQDAIETDAMIKKKTKSSKPSKPEKDKEPRKGKGKSSKK

RFC1 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Cloning and expression of a novel human DNA binding protein, PO-GA. Lu Y, Zeft AS, Riegel AT Biochem Biophys Res Commun June 15, 1993
cDNAs encoding the large subunit of human replication factor C. Bunz F, Kobayashi R, Stillman B Proc Natl Acad Sci U S A Dec. 1, 1993
The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3' processing of mRNA. Lu Y, Riegel AT Gene Aug. 5, 1994
Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. Mossi R, Jonsson ZO, Allen BL, Hardin SH, Hubscher U J Biol Chem Feb. 17, 1997
DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C. Allen BL, Uhlmann F, Gaur LK, Mulder BA, Posey KL, Jones LB, Hardin SH Nucleic Acids Res Sept. 1, 1998
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S Nat Genet Feb. 1, 2004
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
Phosphoproteome analysis of the human mitotic spindle. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R Proc Natl Acad Sci U S A April 4, 2006
A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP Nat Biotechnol Oct. 1, 2006
Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z EMBO J Nov. 1, 2006
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009


Last modification of this entry: Oct. 6, 2010.

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